Iron in PDB 2zyq: Crystal Structure of the Hsac Extradiol Dioxygenase From M. Tuberculosis

All present enzymatic activity of Crystal Structure of the Hsac Extradiol Dioxygenase From M. Tuberculosis:
1.13.11.39;

The structure of Crystal Structure of the Hsac Extradiol Dioxygenase From M. Tuberculosis, PDB code: 2zyq was solved by I.D'angelo, K.C.Yam, L.D.Eltis, N.Strynadka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.00
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	123.737, 123.737, 106.784, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 22.3

The binding sites of Iron atom in the Crystal Structure of the Hsac Extradiol Dioxygenase From M. Tuberculosis (pdb code 2zyq). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of the Hsac Extradiol Dioxygenase From M. Tuberculosis, PDB code: 2zyq:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the Hsac Extradiol Dioxygenase From M. Tuberculosis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of the Hsac Extradiol Dioxygenase From M. Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:12.6 occ:1.00 OE1 A:GLU266 2.0 8.5 1.0 O A:HOH302 2.1 10.3 1.0 NE2 A:HIS145 2.1 11.8 1.0 O A:HOH303 2.2 11.0 1.0 NE2 A:HIS215 2.2 9.3 1.0 CE1 A:HIS145 3.0 9.0 1.0 CD A:GLU266 3.1 9.2 1.0 CE1 A:HIS215 3.2 11.4 1.0 CD2 A:HIS215 3.2 10.6 1.0 CD2 A:HIS145 3.2 10.1 1.0 OH A:TYR256 3.6 12.2 1.0 OE2 A:GLU266 3.6 11.5 1.0 CB A:MET217 3.9 8.8 1.0 NE2 A:HIS200 4.0 11.2 1.0 O A:HOH325 4.1 13.2 1.0 ND1 A:HIS145 4.2 13.5 1.0 O A:HOH549 4.2 56.8 1.0 CG A:MET217 4.2 9.6 1.0 ND1 A:HIS215 4.3 12.5 1.0 CG A:HIS145 4.3 10.8 1.0 CG A:HIS215 4.3 12.5 1.0 CG A:GLU266 4.4 8.6 1.0 OD2 A:ASP250 4.4 15.4 1.0 CE1 A:HIS247 4.5 14.7 1.0 CZ A:TYR256 4.5 12.5 1.0 CB A:GLU266 4.5 9.8 1.0 CE1 A:HIS200 4.7 10.8 1.0 ND1 A:HIS247 4.7 17.3 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the Hsac Extradiol Dioxygenase From M. Tuberculosis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of the Hsac Extradiol Dioxygenase From M. Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:15.7 occ:1.00 OE1 B:GLU266 2.0 11.1 1.0 NE2 B:HIS145 2.1 8.4 1.0 O B:HOH303 2.2 14.9 1.0 NE2 B:HIS215 2.2 12.0 1.0 O B:HOH304 2.3 11.9 1.0 CE1 B:HIS145 2.9 9.4 1.0 CE1 B:HIS215 3.1 12.8 1.0 CD B:GLU266 3.1 8.4 1.0 CD2 B:HIS145 3.2 11.7 1.0 CD2 B:HIS215 3.3 12.2 1.0 OE2 B:GLU266 3.6 13.2 1.0 OH B:TYR256 3.7 12.1 1.0 CB B:MET217 4.0 11.0 1.0 O B:HOH312 4.0 14.9 1.0 ND1 B:HIS145 4.1 11.2 1.0 NE2 B:HIS200 4.2 11.3 1.0 CG B:MET217 4.2 11.0 1.0 ND1 B:HIS215 4.2 10.2 1.0 CG B:HIS145 4.3 11.5 1.0 OD2 B:ASP250 4.3 15.7 1.0 CG B:GLU266 4.4 8.1 1.0 CG B:HIS215 4.4 12.4 1.0 CE1 B:HIS247 4.5 14.1 1.0 CB B:GLU266 4.5 11.8 1.0 CZ B:TYR256 4.7 14.0 1.0 CE1 B:HIS200 4.7 11.8 1.0 ND1 B:HIS247 4.7 16.9 1.0 CG2 B:VAL147 4.9 16.1 1.0

K.C.Yam, I.D'angelo, R.Kalscheuer, H.Zhu, J.X.Wang, V.Snieckus, L.H.Ly, P.J.Converse, W.R.Jacobs, N.Strynadka, L.D.Eltis. Studies of A Ring-Cleaving Dioxygenase Illuminate the Role of Cholesterol Metabolism in the Pathogenesis of Mycobacterium Tuberculosis. Plos Pathog. V. 5 E1000 2009.
ISSN: ISSN 1553-7366
PubMed: 19300498
DOI: 10.1371/JOURNAL.PPAT.1000344